NFKB1_CHICK
ID NFKB1_CHICK Reviewed; 983 AA.
AC Q04861; E1C613; F1NU28; O13075;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Nuclear factor NF-kappa-B p105 subunit;
DE AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1;
DE Contains:
DE RecName: Full=Nuclear factor NF-kappa-B p50 subunit;
GN Name=NFKB1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1533881; DOI=10.1128/jvi.66.6.3758-3767.1992;
RA Capobianco A.J., Chang D., Mosialos G., Gilmore T.D.;
RT "p105, the NF-kappa B p50 precursor protein, is one of the cellular
RT proteins complexed with the v-Rel oncoprotein in transformed chicken spleen
RT cells.";
RL J. Virol. 66:3758-3767(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Spleen;
RX PubMed=7916720; DOI=10.1016/0378-1119(93)90645-j;
RA Ikeda T., Honjo K., Hirota Y., Onodera T.;
RT "Isolation of the chicken NF-kappa B p65 subunit-encoding cDNA and
RT characterization of its products.";
RL Gene 133:237-242(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Embryonic fibroblast;
RX PubMed=9233775; DOI=10.1038/sj.onc.1201162;
RA Cabannes E., Vives M.F., Bedard P.A.;
RT "Transcriptional and post-transcriptional regulation of kappaB-controlled
RT genes by pp60v-src.";
RL Oncogene 15:29-43(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: P105 is the precursor of the p50 subunit of the nuclear
CC factor NF-kappa-B, which binds to the kappa-B consensus sequence 5'-
CC GGRNNYYCC-3', located in the enhancer region of genes involved in
CC immune response and acute phase reactions. The precursor protein itself
CC does not bind to DNA.
CC -!- SUBUNIT: Active NF-kappa-B is a heterodimer of an about 50 kDa DNA-
CC binding subunit and the weak DNA-binding subunit p65. Two heterodimers
CC might form a labile tetramer.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also found
CC in the cytoplasm in an inactive form complexed to an inhibitor (I-
CC kappa-B).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q04861-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04861-2; Sequence=VSP_042871;
CC Name=3;
CC IsoId=Q04861-3; Sequence=VSP_042872;
CC -!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic
CC retention, inhibition of DNA-binding by p50 homodimers, and/or
CC transcription activation.
CC -!- PTM: While translation occurs, the particular unfolded structure after
CC the GRR repeat promotes the generation of p50 making it an acceptable
CC substrate for the proteasome. This process is known as cotranslational
CC processing. The processed form is active and the unprocessed form acts
CC as an inhibitor (I kappa B-like), being able to form cytosolic
CC complexes with NF-kappa B, trapping it in the cytoplasm. Complete
CC folding of the region downstream of the GRR repeat precludes processing
CC (By similarity). {ECO:0000250}.
CC -!- PTM: S-nitrosylation of Cys-66 affects DNA binding. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58343.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB58343.1; Type=Erroneous translation; Note=Wrong genetic code used for translating the sequence.; Evidence={ECO:0000305};
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DR EMBL; M86930; AAA49000.1; -; mRNA.
DR EMBL; D13719; BAA02872.1; -; mRNA.
DR EMBL; AF000241; AAB58343.1; ALT_SEQ; mRNA.
DR EMBL; AADN02031451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A41996; A41996.
DR RefSeq; NP_990465.1; NM_205134.1.
DR RefSeq; XP_015140901.1; XM_015285415.1. [Q04861-3]
DR AlphaFoldDB; Q04861; -.
DR SMR; Q04861; -.
DR STRING; 9031.ENSGALP00000036814; -.
DR PaxDb; Q04861; -.
DR Ensembl; ENSGALT00000037607; ENSGALP00000036814; ENSGALG00000012304. [Q04861-3]
DR Ensembl; ENSGALT00000086369; ENSGALP00000060090; ENSGALG00000012304. [Q04861-3]
DR GeneID; 396033; -.
DR KEGG; gga:396033; -.
DR CTD; 4790; -.
DR VEuPathDB; HostDB:geneid_396033; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000158625; -.
DR HOGENOM; CLU_004343_1_0_1; -.
DR InParanoid; Q04861; -.
DR OMA; MTWIPRK; -.
DR OrthoDB; 916931at2759; -.
DR Reactome; R-GGA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-GGA-1227892; TRAF6 mediated NF-kB activation.
DR Reactome; R-GGA-434001; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR Reactome; R-GGA-434131; NFkB activation mediated by RIP1 complexed with activated TLR3.
DR Reactome; R-GGA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR PRO; PR:Q04861; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000012304; Expressed in granulocyte and 13 other tissues.
DR ExpressionAtlas; Q04861; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01177; IPT_NFkappaB; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR033926; IPT_NFkappaB.
DR InterPro; IPR030503; NF-kB_p105.
DR InterPro; IPR000451; NFkB/Dor.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR030492; RHD_CS.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR24169; PTHR24169; 1.
DR PANTHER; PTHR24169:SF9; PTHR24169:SF9; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR00057; NFKBTNSCPFCT.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS01204; REL_1; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; ANK repeat; Cytoplasm; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; S-nitrosylation;
KW Transcription; Transcription regulation.
FT CHAIN 1..983
FT /note="Nuclear factor NF-kappa-B p105 subunit"
FT /id="PRO_0000030316"
FT CHAIN 1..?
FT /note="Nuclear factor NF-kappa-B p50 subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030317"
FT DOMAIN 47..372
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REPEAT 540..569
FT /note="ANK 1"
FT REPEAT 579..608
FT /note="ANK 2"
FT REPEAT 612..641
FT /note="ANK 3"
FT REPEAT 648..677
FT /note="ANK 4"
FT REPEAT 682..712
FT /note="ANK 5"
FT REPEAT 716..745
FT /note="ANK 6"
FT REPEAT 769..799
FT /note="ANK 7"
FT DOMAIN 804..891
FT /note="Death"
FT REGION 377..397
FT /note="GRR"
FT REGION 423..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 365..370
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 433..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 342
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 970
FT /note="Y -> YG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1533881,
FT ECO:0000303|PubMed:9233775"
FT /id="VSP_042871"
FT VAR_SEQ 971..983
FT /note="RKAQCKAVIYLTR -> GQESSVQSSYIPN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7916720"
FT /id="VSP_042872"
FT CONFLICT 111
FT /note="V -> R (in Ref. 1; AAA49000)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="A -> R (in Ref. 1; AAA49000 and 3; AAB58343)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="V -> I (in Ref. 2; BAA02872)"
FT /evidence="ECO:0000305"
FT CONFLICT 708..710
FT /note="ADV -> VDA (in Ref. 2; BAA02872)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="L -> H (in Ref. 3; AAB58343)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="R -> Q (in Ref. 1; AAA49000)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="V -> G (in Ref. 1; AAA49000)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="L -> F (in Ref. 1; AAA49000)"
FT /evidence="ECO:0000305"
FT CONFLICT 898..899
FT /note="SH -> IY (in Ref. 2; BAA02872)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="N -> K (in Ref. 1; AAA49000)"
FT /evidence="ECO:0000305"
FT CONFLICT 938
FT /note="S -> T (in Ref. 3; AAB58343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 983 AA; 107992 MW; B8885C7716393285 CRC64;
MAGEDPYIMG VSDPQMFAMD QLMGMSTIFN NTGYITSDLP LRTADGPYLQ IIEQPKQRGF
RFRYVCEGPS HGGLPGASSE KNKKSYPQVK ICNYVGPAKV IVQLVTNGKY VHLHAHSLVG
KFCEDGVCTV NAGPKDMVVG FANLGILHVT KKKVFETLET RMIDACKKGY NPGLLVHPEL
GYLQAEGCGD RQLTEREREI IRQAAVQQTK EMDLSVVRLM FTAFLPDSNG GFTRRLDPVI
SDAIYDSKAP NASNLKIVRM DRTAGCVTGG EEIYLLCDKV QKDDIQIRFY EEDENGGMWE
GFGDFSPTDV HRQFAIVFKT PKYRDVNITK PASVFVQLRR KSDLETSEPK PFLYYPEIKD
KEEVQRKRQK LMPNFSDGYG GGSGAGGGGM FGGGGGGAGS GFSYPSYGYS AFGGMHFHPG
TTKSNAGMKH ELSNSTVKKD EESSDKQSDK WDTKHDVKVE TVEKNECRTS GHNEEKEDAS
LCCKDEGNKP KCGCQDGLFL EKAMQLAKRH CNALFDYAVT GDVRMLLAVQ RHLTAVQDDN
GDNVLHLSII HLHRELVKNL LEVMPDMNYN NIINMRNDLY QTPLHLAVIT KQAEVVEDLL
KAGANVNLLD RHGNSVLHLA AAEGDDKILS LLLKHQKASS MIDLSNGEGL SAIHMVVTAN
SLSCLKLLIA AGVDVNAQEQ KSGRTALHLA VEQENVPLAG CLLLEGDADV DSTTYDGTTP
LHIAAGRGFT KLAAVLKAAG ADPHVENFEP LFDVEEDVKD DDDDEGIVPG TTPLDMAANW
EVYDILNGKP YIAAAAVSED LLSQGPLREL NESSKQQLYK LLETPDPSKN WSTLAEKLGL
GILNNAFRLS PSPSKTLLDN YKISGGTVQE LIAALTQMDH TEAIEVIQKA LSSSQRQSHQ
EDNTIEAFPS LSPTSFAKEE TGELYNHKFQ DPESTCDSGV ETSFRKLSFT YSDSLNSKSS
ITLSKMTLGY RKAQCKAVIY LTR
